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Crystal structure and function of C-terminal Sau3AI domain

Authors :
Xu, Chun-Yan
Yu, Feng
Xu, Si-Jie
Ding, Yu
Sun, Li-Hua
Tang, Lin
Hu, Xiao-Jian
Zhang, Zhi-Hong
He, Jian-Hua
Source :
BBA - Proteins & Proteomics. Jan2009, Vol. 1794 Issue 1, p118-123. 6p.
Publication Year :
2009

Abstract

Abstract: Sau3AI is a type II restriction enzyme that recognizes the 5′-GATC-3′ sequence in double-strand DNA and cleaves at 5′ to the G residue. The C-terminal domain of Sau3AI (Sau3AI-C), which contains amino acids from 233 to 489, was crystallized and its structure was solved by using the Multi-wavelength Anomalous Diffraction method. The Sau3AI-C structure at 1.9 Å resolution is similar to the structure of MutH, a DNA mismatch repair protein that shares high sequence similarity with the N-terminal Sau3AI domain. The functional analysis shows that Sau3AI-C can bind DNA with one recognition sequence but has no cleavage activity. These results indicate that Sau3AI is a pseudo-dimer belonging to the type IIe restriction enzymes and the Sau3AI-C is the allosteric effector domain that assists DNA binding and cleavage. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
15709639
Volume :
1794
Issue :
1
Database :
Academic Search Index
Journal :
BBA - Proteins & Proteomics
Publication Type :
Academic Journal
Accession number :
35507461
Full Text :
https://doi.org/10.1016/j.bbapap.2008.09.008